Rxivist logo

EVfold.org: Evolutionary Couplings and Protein 3D Structure Prediction

By Robert Sheridan, Robert J. Fieldhouse, Sikander Hayat, Yichao Sun, Yevgeniy Antipin, Li Yang, Thomas Hopf, Debora S. Marks, Chris Sander

Posted 02 Jul 2015
bioRxiv DOI: 10.1101/021022

Recently developed maximum entropy methods infer evolutionary constraints on protein function and structure from the millions of protein sequences available in genomic databases. The EVfold web server (at EVfold.org) makes these methods available to predict functional and structural interactions in proteins. The key algorithmic development has been to disentangle direct and indirect residue-residue correlations in large multiple sequence alignments and derive direct residue-residue evolutionary couplings (EVcouplings or ECs). For proteins of unknown structure, distance constraints obtained from evolutionarily couplings between residue pairs are used to de novo predict all-atom 3D structures, often to good accuracy. Given sufficient sequence information in a protein family, this is a major advance toward solving the problem of computing the native 3D fold of proteins from sequence information alone. Availability: EVfold server at http://evfold.org/ Contact: evfoldtest@gmail.com

Download data

  • Downloaded 3,923 times
  • Download rankings, all-time:
    • Site-wide: 2,247 out of 118,130
    • In bioinformatics: 224 out of 9,572
  • Year to date:
    • Site-wide: 7,815 out of 118,130
  • Since beginning of last month:
    • Site-wide: 6,650 out of 118,130

Altmetric data

Downloads over time

Distribution of downloads per paper, site-wide


Sign up for the Rxivist weekly newsletter! (Click here for more details.)